Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.
Autor(a) principal: | |
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Data de Publicação: | 2023 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10174/36142 |
Resumo: | ShK domain-containing proteins are peptides found in different parasitic and venomous organisms. From a previous transcriptomic dataset from Bursaphelenchus xylophilus, a plant-endoparasitic nematode that infects forest tree species, we identified 96 transcripts potentially as ShK domain-containing proteins with unknown function in the nematode genome. This study aimed to characterize and explore the functional role of genes encoding ShK domain-containing proteins in B. xylophilus biology. We selected and functionally analyzed nine candidate genes specific from B. xylophilus. In situ hybridization revealed expression of one B. xylophilus ShK in the pharyngeal gland cells, suggesting their delivery into host cells. Most of the transcripts are highly expressed during infection and showed a significant upregulation in response to peroxide products compared to the nematode catalase enzymes. We reported for the first time, the potential involvement of ShK domain genes in oxidative stress, suggesting that these proteins may have an important role protecting or modulating the reactive oxygen species (ROS) activity of the host plant during parasitism. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus.molecular plant-nematode interactionparasitismpinewood nematodeShK domain-containing proteinoxidative stressShK domain-containing proteins are peptides found in different parasitic and venomous organisms. From a previous transcriptomic dataset from Bursaphelenchus xylophilus, a plant-endoparasitic nematode that infects forest tree species, we identified 96 transcripts potentially as ShK domain-containing proteins with unknown function in the nematode genome. This study aimed to characterize and explore the functional role of genes encoding ShK domain-containing proteins in B. xylophilus biology. We selected and functionally analyzed nine candidate genes specific from B. xylophilus. In situ hybridization revealed expression of one B. xylophilus ShK in the pharyngeal gland cells, suggesting their delivery into host cells. Most of the transcripts are highly expressed during infection and showed a significant upregulation in response to peroxide products compared to the nematode catalase enzymes. We reported for the first time, the potential involvement of ShK domain genes in oxidative stress, suggesting that these proteins may have an important role protecting or modulating the reactive oxygen species (ROS) activity of the host plant during parasitism.MDPI2024-01-18T10:51:16Z2024-01-182023-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10174/36142http://hdl.handle.net/10174/36142porMendonça, M., Vicente, C.S.L., Espada, M. Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. 2023. pp:1-16. 10.20944/preprints202312.0388.v1https://www.preprints.org/manuscript/202312.0388/v1maria.silva@uevora.ptcvicente@uevora.ptmespada@uevora.pt581doi: 10.20944/preprints202312.0388.v1Mendonça, MadalenaVicente, CláudiaEspada, Margaridainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-01-23T01:46:49Zoai:dspace.uevora.pt:10174/36142Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T01:56:33.129906Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
title |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
spellingShingle |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. Mendonça, Madalena molecular plant-nematode interaction parasitism pinewood nematode ShK domain-containing protein oxidative stress |
title_short |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
title_full |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
title_fullStr |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
title_full_unstemmed |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
title_sort |
Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. |
author |
Mendonça, Madalena |
author_facet |
Mendonça, Madalena Vicente, Cláudia Espada, Margarida |
author_role |
author |
author2 |
Vicente, Cláudia Espada, Margarida |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Mendonça, Madalena Vicente, Cláudia Espada, Margarida |
dc.subject.por.fl_str_mv |
molecular plant-nematode interaction parasitism pinewood nematode ShK domain-containing protein oxidative stress |
topic |
molecular plant-nematode interaction parasitism pinewood nematode ShK domain-containing protein oxidative stress |
description |
ShK domain-containing proteins are peptides found in different parasitic and venomous organisms. From a previous transcriptomic dataset from Bursaphelenchus xylophilus, a plant-endoparasitic nematode that infects forest tree species, we identified 96 transcripts potentially as ShK domain-containing proteins with unknown function in the nematode genome. This study aimed to characterize and explore the functional role of genes encoding ShK domain-containing proteins in B. xylophilus biology. We selected and functionally analyzed nine candidate genes specific from B. xylophilus. In situ hybridization revealed expression of one B. xylophilus ShK in the pharyngeal gland cells, suggesting their delivery into host cells. Most of the transcripts are highly expressed during infection and showed a significant upregulation in response to peroxide products compared to the nematode catalase enzymes. We reported for the first time, the potential involvement of ShK domain genes in oxidative stress, suggesting that these proteins may have an important role protecting or modulating the reactive oxygen species (ROS) activity of the host plant during parasitism. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-12-01T00:00:00Z 2024-01-18T10:51:16Z 2024-01-18 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10174/36142 http://hdl.handle.net/10174/36142 |
url |
http://hdl.handle.net/10174/36142 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
Mendonça, M., Vicente, C.S.L., Espada, M. Functional characterization of ShK domain-containing protein in the plant-parasitic nematode Bursaphelenchus xylophilus. 2023. pp:1-16. 10.20944/preprints202312.0388.v1 https://www.preprints.org/manuscript/202312.0388/v1 maria.silva@uevora.pt cvicente@uevora.pt mespada@uevora.pt 581 doi: 10.20944/preprints202312.0388.v1 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
MDPI |
publisher.none.fl_str_mv |
MDPI |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799137054180769792 |